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GPA1_PEA
ID   GPA1_PEA                Reviewed;         384 AA.
AC   O04278;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Guanine nucleotide-binding protein alpha-1 subunit;
DE            Short=GP-alpha-1;
GN   Name=GPA1; Synonyms=GA1;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska; TISSUE=Apical bud;
RX   PubMed=10476071; DOI=10.1046/j.1365-313x.1999.00516.x;
RA   Marsh J.F. III, Kaufman L.S.;
RT   "Cloning and characterisation of PGA1 and PGA2: two G protein alpha-
RT   subunits from pea that promote growth in the yeast Saccharomyces
RT   cerevisiae.";
RL   Plant J. 19:237-247(1999).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site.
CC   -!- DOMAIN: The helical domain (69-189) is required for self-activation.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR   EMBL; U97043; AAB57825.1; -; mRNA.
DR   AlphaFoldDB; O04278; -.
DR   SMR; O04278; -.
DR   PRIDE; O04278; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IEA:InterPro.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002976; Plant_Gprotein_alpha.
DR   PANTHER; PTHR10218; PTHR10218; 1.
DR   PANTHER; PTHR10218:SF333; PTHR10218:SF333; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR01242; GPROTEINAPLT.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Lipoprotein; Magnesium; Metal-binding; Myristate;
KW   Nucleotide-binding; Palmitate; Transducer.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..384
FT                   /note="Guanine nucleotide-binding protein alpha-1 subunit"
FT                   /id="PRO_0000203623"
FT   DOMAIN          38..384
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          41..54
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          186..194
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          215..224
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          284..291
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          354..359
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   BINDING         46..53
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         188..194
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         219..223
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         288..291
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
FT   LIPID           5
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   384 AA;  44700 MW;  B7797AA22592F39C CRC64;
     MGLLCSKSNR YNDAKAEENA QTAEIERRIE LETKAEKHIR KLLLLGAGES GKSTIFKQIK
     LLFQTGFDEA ELKSYLPVVH ANVYQTIKLL HDGSKEFAQN DVDFSKYVIS TENKDIGEKL
     SEIGGRLDYP RLTKELAQEI ESIWKDAAIQ ETYARGNELQ VPDCTHYFME NLQRLSDANY
     VPTKEDVLLA RVRTTGVVEI QFSPVGENKK SGEVYRLFDV GGQRNERRKW IHLFEGVSAV
     IFCVAISEYD QTLFEDENKN RMMETKELFE WVLKQQCFEK TSFMLFLNKF DIFEKKILDV
     PLNVCEWFKD YQPVSTGKQE IEHAYEFVKK KFEESYFQST APDSVDRVFK IYRTTALDQK
     VVKKTFKLVD ETLRRRNLFE AGLL
 
 
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